Work

Crystallization and preliminary X-ray analysis of the complex between aBacillus subtilisα/β-type small acid-soluble spore protein and DNA

Year: 2007

Type: article

Abstract: An engineered variant of an alpha/beta-type small acid-soluble spore protein (SASP) from Bacillus subtilis was crystallized in a complex with a ten-base-pair double-stranded DNA by the hanging-drop vapor-diffusion method using ammonium sulfate as a precipitating agent. Crystals grew at 281 K using sodium cacodylate buffer pH 5.5 and these crystals diffracted X-rays to beyond 2.4 A resolution using synchrotron radiation. The crystallized complex contains two or three SASP molecules bound to one DNA molecule. The crystals belong to the hexagonal space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 87.0, c = 145.4 A, alpha = beta = 90.0, gamma = 120.0 degrees. Diffraction data were 96.6% complete to 2.4 A resolution, with an R(sym) of 8.5%. Structure solution by the multiwavelength/single-wavelength anomalous dispersion method using isomorphous crystals of selenomethionine-labeled protein is in progress.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309107022750

Authors: Daniela Bumbaca, Jeffrey Kosman, Peter Setlow, R. Keith Henderson, Mark J. Jedrzejas

Institutions: UConn Health, Lawrence Berkeley National Laboratory

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze